Expression, purification and crystallization of human bile acid-coA:amino acidN-acyltransferase (BAAT)

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Purification and characterization of bile acid-CoA:amino acid N-acyltransferase from human liver.

The bile acid-conjugating enzyme, bile acid-CoA: amino acid N-acyltransferase, was purified 480-fold from the soluble fraction of homogenized frozen human liver. Purification was accomplished by a combination of anion exchange chromatography, chromatofocusing, glycocholate-AH-Sepharose affinity chromatography, and high performance liquid chromatography (HPLC) gel filtration. Following purificat...

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Purification and characterization of bile acid-CoA:amino acid N-acyltransferase from rat liver.

An in vitro study of bile acid-CoA:amino acid N-acyltransferase activity of rat liver was undertaken in order to determine whether separate amino acid-specific enzymes catalyzed the formation of glycine and taurine conjugates of bile acids as postulated by others. Polyacrylamide gel electrophoresis of 200-fold purified enzyme localized the glycine- and taurine-dependent activities to a single b...

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Cloning, expression, and chromosomal localization of mouse liver bile acid CoA:amino acid N-acyltransferase.

A mouse liver lambda Zap XR cDNA library was screened using the coding region of human bile acid CoA:amino acid N-acyltransferase (BAT) cDNA as a probe. Ten positive clones were isolated and purified, two of which apparently possessed complete open reading frames for BAT based on sequence analysis of the ends of the cDNAs. One clone (mBAT#9) was selected for sequence analysis and characterizati...

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Cloning, Expression, Purification and CD Analysis of Recombinant Human Betatrophin

Betatrophin is a member of the angiopoietin-like (ANGPTL) family that has been implicated in both triglyceride and glucose metabolism. The physiological functions and molecular targets of this protein remain largely unknown; hence, a purified available protein would aid study of the exact role of betatrophin in lipid or glucose metabolism. In this study, we cloned the full-length cDNA of betatr...

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Rat liver bile acid CoA:amino acid N-acyltransferase: expression, characterization, and peroxisomal localization.

Bile acid CoA:amino acid N-acyltransferase (BAT) is responsible for the amidation of bile acids with the amino acids taurine and glycine. Rat liver BAT (rBAT) cDNA was isolated from a rat liver lambdaZAP cDNA library and expressed in Sf9 insect cells using a baculoviral vector. rBAT displayed 65% amino acid sequence homology with human BAT (hBAT) and 85% homology with mouse BAT (mBAT). Similar ...

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ژورنال

عنوان ژورنال: Acta Crystallographica Section A Foundations of Crystallography

سال: 2009

ISSN: 0108-7673

DOI: 10.1107/s0108767309096834